Kinetic Binding Analysis of Aptamers Targeting HIV-1 Proteins by a Combination of a Microbalance Array and Mass Spectrometry (MAMS)

2009 ◽  
Vol 8 (7) ◽  
pp. 3568-3577 ◽  
Author(s):  
Thomas M. A. Gronewold ◽  
Antje Baumgartner ◽  
Jessica Hierer ◽  
Saleta Sierra ◽  
Michael Blind ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Analysis ◽  
Hiv 1

Loss of macrophage-secreted lysozyme in HIV-1-associated dementia detected by SELDI-TOF mass spectrometry

AIDS ◽  
2004 ◽  
Vol 18 (7) ◽  
pp. 1009-1012 ◽  
Author(s):  
Bing Sun ◽  
Hans C Rempel ◽  
Lynn Pulliam
Keyword(s):  
Mass Spectrometry ◽  
Hiv 1

scholarly journals Mass Spectrometry Approach and ELISA Reveal the Effect of Codon Optimization on N-Linked Glycosylation of HIV-1 gp120

2014 ◽  
Vol 13 (12) ◽  
pp. 5801-5811 ◽  
Author(s):  
Kourosh Honarmand Ebrahimi ◽  
Graham M. West ◽  
Ricardo Flefil
Keyword(s):  
Mass Spectrometry ◽  
Codon Optimization ◽  
Hiv 1

HIV-1 Tat Peptide Binding to TAR RNA by Electrospray Ionization Mass Spectrometry

1997 ◽  
Vol 69 (24) ◽  
pp. 5130-5135 ◽  
Author(s):  
Kristin A. Sannes-Lowery ◽  
Peifeng Hu ◽  
David P. Mack ◽  
Houng-Yau Mei ◽  
Joseph A. Loo
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Peptide Binding ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Tat Peptide ◽  
Tar Rna ◽  
Hiv 1

scholarly journals Structure and binding analysis of active site inhibitors targeting HIV-1 RNase H

2011 ◽  
Vol 67 (a1) ◽  
pp. C303-C303
Author(s):  
E. B. Lansdon ◽  
Q. Liu ◽  
S. A. Leavitt ◽  
M. Balakrishnan ◽  
J. K. Perry ◽  
...  
Keyword(s):  
Active Site ◽  
Rnase H ◽  
Binding Analysis ◽  
Hiv 1

scholarly journals Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity

2007 ◽  
Vol 69 (2) ◽  
pp. 270-284 ◽  
Author(s):  
Jared R. Auclair ◽  
Karin M. Green ◽  
Shivender Shandilya ◽  
James E. Evans ◽  
Mohan Somasundaran ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Analysis ◽  
Viral Infectivity ◽  
Ordered Structure ◽  
Spectrometry Analysis ◽  
Hiv 1

scholarly journals Characterization of Glycosylation Profiles of HIV-1 Transmitted/Founder Envelopes by Mass Spectrometry

2011 ◽  
Vol 85 (16) ◽  
pp. 8270-8284 ◽  
Author(s):  
E. P. Go ◽  
G. Hewawasam ◽  
H.-X. Liao ◽  
H. Chen ◽  
L.-H. Ping ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Hiv 1

scholarly journals HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase

2000 ◽  
Vol 346 (2) ◽  
pp. 305-311 ◽  
Author(s):  
David A. DAVIS ◽  
Fonda M. NEWCOMB ◽  
Jackob MOSKOVITZ ◽  
Paul T. WINGFIELD ◽  
Stephen J. STAHL ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Peptide Mapping ◽  
Hiv Protease ◽  
Reversible Inactivation ◽  
Dimer Interface ◽  
Oxidative Inactivation ◽  
Human Immunodeficiency Viruses ◽  
Methionine Residues ◽  
Hiv 1

Human immunodeficiency viruses encode a homodimeric protease that is essential for the production of infectious virus. Previous studies have shown that HIV-1 protease is susceptible to oxidative inactivation at the dimer interface at Cys-95, a process that can be reversed both chemically and enzymically. Here we demonstrate a related yet distinct mechanism of reversible inactivation of the HIV-2 protease. Exposure of the HIV-2 protease to H2O2 resulted in conversion of the two methionine residues (Met-76 and Met-95) to methionine sulphoxide as determined by amino acid analysis and mass spectrometry. This oxidation completely inactivated protease activity. However, the activity could be restored (up to 40%) after exposure of the oxidized protease to methionine sulphoxide reductase. This treatment resulted in the reduction of methionine sulphoxide 95 but not methionine sulphoxide 76 to methionine, as determined by peptide mapping/mass spectrometry. We also found that exposure of immature HIV-2 particles to H2O2 led to the inhibition of polyprotein processing in maturing virus particles comparable to that demonstrated for HIV-1 particles. Thus oxidative inactivation of the HIV protease in vitro and in maturing viral particles is not restricted to the type 1 proteases. These studies indicate that two distinct retroviral proteases are susceptible to inactivation after a very minor modification at residue 95 of the dimer interface and suggest that the dimer interface might be a viable target for the development of novel protease inhibitors.

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